P07330 (CHEB_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 124.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Chemotaxis response regulator protein-glutamate methylesterase EC=3.1.1.61 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 349 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. HAMAP-Rule MF_00099 |
| Catalytic activity | Protein L-glutamate O(5)-methyl ester + H2O = protein L-glutamate + methanol. HAMAP-Rule MF_00099 |
| Subcellular location | |
| Domain | The N-terminal regulatory domain inhibits the activity of the C-terminal effector domain. HAMAP-Rule MF_00099 |
| Post-translational modification | Phosphorylated by CheA. Phosphorylation suppresses the inhibitory activity of the N-terminal domain. Ref.5 |
| Sequence similarities | Contains 1 cheB-type methylesterase domain. Contains 1 response regulatory domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Chemotaxis |
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | chemotaxis Inferred from mutant phenotype PubMed 4895809. Source: EcoliWiki intracellular signal transductionInferred from electronic annotation. Source: GOC regulation of transcription, DNA-dependentInferred from electronic annotation. Source: InterPro sensory perception of chemical stimulusInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | phosphorelay response regulator activity Inferred from electronic annotation. Source: InterPro protein-glutamate methylesterase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 349 | 349 | Chemotaxis response regulator protein-glutamate methylesterase HAMAP-Rule MF_00099 | PRO_0000157992 | |||||
Regions | |||||||||
| Domain | 5 – 122 | 118 | Response regulatory | ||||||
| Domain | 152 – 344 | 193 | CheB-type methylesterase | ||||||
Sites | |||||||||
| Active site | 164 | 1 | By similarity | ||||||
| Active site | 190 | 1 | By similarity | ||||||
| Active site | 286 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 56 | 1 | 4-aspartylphosphate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 96 | 1 | A → P in AAA23569. Ref.1 | ||||||
| Sequence conflict | 125 | 1 | E → Q in AAA23569. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli." Mutoh N., Simon M.I. J. Bacteriol. 165:161-166(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. Horiuchi T.DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis." Hess J.F., Oosawa K., Kaplan N., Simon M.I. Cell 53:79-87(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M13463 Genomic DNA. Translation: AAA23569.1. U00096 Genomic DNA. Translation: AAC74953.1. AP009048 Genomic DNA. Translation: BAA15699.1. |
| PIR | XYECEB. D25195. |
| RefSeq | NP_416397.1. NC_000913.2. YP_490145.1. NC_007779.1. |
3D structure databases | |
| ProteinModelPortal | P07330. |
| SMR | P07330. Positions 1-347. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-9272N. |
| IntAct | P07330. 10 interactions. |
| STRING | 511145.b1883. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAC74953; AAC74953; b1883. BAA15699; BAA15699; BAA15699. |
| GeneID | 12931722. 946394. |
| KEGG | ecj:Y75_p1859. eco:b1883. |
| PATRIC | 32119093. VBIEscCol129921_1964. |
Organism-specific databases | |
| EchoBASE | EB0145. |
| EcoGene | EG10147. cheB. |
Phylogenomic databases | |
| eggNOG | COG2201. |
| HOGENOM | HOG000151423. |
| KO | K03412. |
| OMA | EAPVNRH. |
| ProtClustDB | PRK00742. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:CHEB-MONOMER. ECOL316407:JW1872-MONOMER. MetaCyc:CHEB-MONOMER. |
| BRENDA | 3.1.1.61. 2026. |
Gene expression databases | |
| Genevestigator | P07330. |
Family and domain databases | |
| Gene3D | 3.40.50.180. 1 hit. |
| HAMAP | MF_00099. CheB_methylest. |
| InterPro | IPR011006. CheY-like_superfamily. IPR008248. Sig_transdc_resp-reg_CheB. IPR000673. Sig_transdc_resp-reg_Me-estase. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view] |
| Pfam | PF01339. CheB_methylest. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view] |
| PIRSF | PIRSF000876. RR_chemtxs_CheB. 1 hit. |
| SMART | SM00448. REC. 1 hit. [Graphical view] |
| SUPFAM | SSF52738. Chemotax_RR_pGlu_Me-esterase. 1 hit. SSF52172. CheY_like. 1 hit. |
| PROSITE | PS50122. CHEB. 1 hit. PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CHEB_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P07330 Secondary accession number(s): P78070 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| SIMILARITY comments Index of protein domains and families |

Clusters with
